Magnesium in PDB 3tba: Structure of Yeast Ribonucleotide Reductase 1 Q288A with Dgtp and Adp

All present enzymatic activity of Structure of Yeast Ribonucleotide Reductase 1 Q288A with Dgtp and Adp:
1.17.4.1;

The structure of Structure of Yeast Ribonucleotide Reductase 1 Q288A with Dgtp and Adp, PDB code: 3tba was solved by M.F.Ahmad, P.S.Kaushal, Q.Wan, S.R.Wijeratna, M.Huang, C.Dealwis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.13 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	107.772, 118.086, 67.710, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 26.4

The binding sites of Magnesium atom in the Structure of Yeast Ribonucleotide Reductase 1 Q288A with Dgtp and Adp (pdb code 3tba). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Yeast Ribonucleotide Reductase 1 Q288A with Dgtp and Adp, PDB code: 3tba:

Magnesium binding site 1 out of 1 in the Structure of Yeast Ribonucleotide Reductase 1 Q288A with Dgtp and Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Yeast Ribonucleotide Reductase 1 Q288A with Dgtp and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg889 b:69.1 occ:1.00 O1B A:DGT890 2.2 54.1 1.0 O1A A:DGT890 2.4 50.4 1.0 O2G A:DGT890 2.8 60.3 1.0 PB A:DGT890 3.6 55.0 1.0 PA A:DGT890 3.7 50.7 1.0 PG A:DGT890 4.1 60.1 1.0 CB A:SER227 4.1 39.0 1.0 O3A A:DGT890 4.1 54.0 1.0 O3B A:DGT890 4.3 57.7 1.0 O2A A:DGT890 4.5 50.0 1.0 O1G A:DGT890 4.5 62.1 1.0 O2B A:DGT890 4.8 55.1 1.0 O A:ASP226 4.9 41.2 1.0 O5' A:DGT890 5.0 48.7 1.0

M.F.Ahmad, P.S.Kaushal, Q.Wan, S.R.Wijerathna, X.An, M.Huang, C.G.Dealwis. Role of Arginine 293 and Glutamine 288 in Communication Between Catalytic and Allosteric Sites in Yeast Ribonucleotide Reductase. J.Mol.Biol. V. 419 315 2012.
ISSN: ISSN 0022-2836
PubMed: 22465672
DOI: 10.1016/J.JMB.2012.03.014